K2C1_CANLF
ID K2C1_CANLF Reviewed; 619 AA.
AC Q6EIY9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Keratin, type II cytoskeletal 1;
DE AltName: Full=Cytokeratin-1;
DE Short=CK-1;
DE AltName: Full=Epithelial keratin-1;
DE AltName: Full=Keratin-1;
DE Short=K1;
DE AltName: Full=Type-II keratin Kb1;
GN Name=KRT1 {ECO:0000250|UniProtKB:P04264};
GN Synonyms=KER1 {ECO:0000312|EMBL:AAQ83910.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1] {ECO:0000312|EMBL:AAQ83910.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epidermis {ECO:0000269|PubMed:15627753};
RX PubMed=15627753; DOI=10.1159/000081527;
RA Credille K.M., Guyon R., Andre C., Murphy K., Tucker K., Barnhart K.F.,
RA Dunstan R.W.;
RT "Comparative sequence analysis and radiation hybrid mapping of two
RT epidermal type II keratin genes in the dog: keratin 1 and keratin 2e.";
RL Cytogenet. Genome Res. 108:328-332(2005).
CC -!- FUNCTION: May regulate the activity of kinases such as PKC and SRC via
CC binding to integrin beta-1 (ITB1) and the receptor of activated protein
CC C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor
CC for kininogen-1/HMWK (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Heterodimer with KRT10 (By similarity). Two heterodimers
CC of KRT1 and KRT10 form a heterotetramer (By similarity). Forms a
CC heterodimer with KRT14; the interaction is more abundant in the absence
CC of KRT5 (By similarity). Interacts with ITGB1 in the presence of RACK1
CC and SRC, and with RACK1 (By similarity). Interacts with C1QBP; the
CC association represents a cell surface kininogen receptor (By
CC similarity). Interacts with EPPK1; interaction is dependent of higher-
CC order structure of intermediate filament (By similarity).
CC {ECO:0000250|UniProtKB:P04104, ECO:0000250|UniProtKB:P04264}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04264}.
CC Cytoplasm {ECO:0000250|UniProtKB:P04264}.
CC -!- PTM: Undergoes deimination of some arginine residues (citrullination).
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AY318945; AAQ83910.1; -; mRNA.
DR RefSeq; NP_001003392.1; NM_001003392.1.
DR AlphaFoldDB; Q6EIY9; -.
DR SMR; Q6EIY9; -.
DR STRING; 9612.ENSCAFP00000010719; -.
DR PaxDb; Q6EIY9; -.
DR PRIDE; Q6EIY9; -.
DR GeneID; 444857; -.
DR KEGG; cfa:444857; -.
DR CTD; 3848; -.
DR eggNOG; ENOG502QQ2I; Eukaryota.
DR InParanoid; Q6EIY9; -.
DR OrthoDB; 824246at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032449; Keratin_2_1_tail.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR Pfam; PF16210; Keratin_2_tail; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Citrullination; Coiled coil; Cytoplasm;
KW Intermediate filament; Keratin; Membrane; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..619
FT /note="Keratin, type II cytoskeletal 1"
FT /id="PRO_0000278097"
FT DOMAIN 181..494
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..180
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..216
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 217..235
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 236..327
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 328..351
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 352..490
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 491..619
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 559..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..477
FT /evidence="ECO:0000255"
FT COMPBIAS 563..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 434
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 45
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 277
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 519
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 575
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
SQ SEQUENCE 619 AA; 63790 MW; E45A8B709AD0909F CRC64;
MSRHFSSRSG FRSGGGFSSG SAGLVSFQRR TTSSSVRHSG GGGGRFSGGR CGGGGGGGAG
GGGFGSRSLV NLGGSKSISI SVAGGGGGRG GFGGGYGGGG FGGGGFGGGS GGFGLGGGFG
GGGFGGGGFG GGGFGGGGFG GGSFGPVCPP GGIQEVTINQ SLLQPLNVEI DPEIQKVKTR
EREQIKSLNN QFASFIDKVR FLEQQNQVLQ TKWELLQQVD TSTRTHSLEP YFENYISNLR
RRVDQLKSDQ SRMDSELKNM QDLVEDYRNK YEDEINKRTN AENEFVTIKK DVDAAFMNKV
DLQAKVDNLQ QEIDFLTTLY QAELSQMQTQ ISETNVILSM DNNRSLDLDS IISEVKAQYE
EIAQKSKAEA EALYQTKYEE LQITAGKHGD NLKSTKMEIS ELNRVAQRLR SEIDSVKKQI
SALQQSISDA EQRGENALKD AQSKLAELED ALQKAKEDMA RLLRDYQELM NTKLALDMEI
ATYRTLLEGE ESRMSGECAP NVSVSVNTSH TTISGGGGRG GGGFGSVGGG GGYGGGSYGS
GGGSYGSGGG GGGSYGSGGG GGGGYGSSSS SGGHRGGSGG GSRSGGSSGG RGSSSGGIKT
SSGSSSVKFV STSYSRAVR
